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Structural Dynamics of the MscL C-terminal Domain
Navid Bavi1,2, Adam D Martinac1,3, D Marien Cortes4
1Victor Chang Cardiac Research Institute, 405 Liverpool Street, Darlinghurst, New South Wales, 2010, Australia.
Scientific Reports
|December 10, 2017
Summary
The bacterial mechanosensitive channel MscL
Area of Science:
- Structural biology
- Biophysics
- Microbiology
Background:
- The large conductance mechanosensitive channel (MscL) in bacteria functions as an essential osmoprotective valve.
- In its closed state, MscL's C-terminus forms a bundle of five alpha-helices along the molecule's symmetry axis.
Purpose of the Study:
- To investigate the structural dynamics of the EcMscL C-terminus.
- To understand the role of the C-terminus in channel gating and MscL structure stabilization.
Main Methods:
- Site-directed spin labeling electron paramagnetic resonance (SDSL EPR) spectroscopy.
- Computational modeling: molecular dynamics (MD) simulations and finite element (FE) modeling.
Main Results:
- The C-terminus forms an alpha-helical bundle near the five-fold symmetry axis under physiological conditions.
- During channel gating, only the top portion (residues A110-E118) of the C-terminus dissociates.
- The lower part of the C-terminus remains assembled, stabilizing the MscL structure.
Conclusions:
- The C-terminus acts as a molecular sieve and a stabilizer for the oligomeric MscL structure.
- Partial dissociation of the C-terminus is crucial for MscL channel gating dynamics.
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